CPRA_DESHD
ID CPRA_DESHD Reviewed; 445 AA.
AC P81594; B8FW15; Q8RPI9;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=3-chloro-4-hydroxyphenylacetate reductive dehalogenase;
DE EC=3.8.1.-;
DE AltName: Full=C1-OHPA dehalogenase;
DE AltName: Full=O-chlorophenol reductive dehalogenase;
DE Flags: Precursor;
GN Name=cprA; OrderedLocusNames=Dhaf_0737;
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Davis J.K., Tiedje J.M.;
RT "Sequence and transcriptional analysis of reductive dehalogenase genes of
RT Desulfitobacterium.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2;
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
RN [3]
RP PROTEIN SEQUENCE OF 43-66, AND CHARACTERIZATION.
RX PubMed=9781670; DOI=10.1016/s0014-5793(98)01114-4;
RA Christiansen N., Ahring B.K., Wohlfarth G., Diekert G.;
RT "Purification and characterization of the 3-chloro-4-hydroxy-phenylacetate
RT reductive dehalogenase of Desulfitobacterium hafniense.";
RL FEBS Lett. 436:159-162(1998).
CC -!- FUNCTION: Catalyzes the reductive dechlorination of C1-OHPA to 4-
CC hydroxyphenylacetate with reduced methyl viologen as the electron
CC donor.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster.;
CC -!- COFACTOR:
CC Name=corrinoid; Xref=ChEBI:CHEBI:33913;
CC Note=Corrinoid.;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
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DR EMBL; AF403182; AAL87763.1; -; Genomic_DNA.
DR EMBL; CP001336; ACL18801.1; -; Genomic_DNA.
DR RefSeq; WP_015942994.1; NC_011830.1.
DR AlphaFoldDB; P81594; -.
DR SMR; P81594; -.
DR EnsemblBacteria; ACL18801; ACL18801; Dhaf_0737.
DR KEGG; dhd:Dhaf_0737; -.
DR HOGENOM; CLU_036586_1_0_9; -.
DR Proteomes; UP000007726; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR012832; RDH.
DR InterPro; IPR028894; RDH_dom.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF13486; Dehalogenase; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR TIGRFAMs; TIGR02486; RDH; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Direct protein sequencing; Hydrolase; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Repeat; Signal.
FT SIGNAL 1..42
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:9781670"
FT CHAIN 43..445
FT /note="3-chloro-4-hydroxyphenylacetate reductive
FT dehalogenase"
FT /id="PRO_0000020991"
FT DOMAIN 320..350
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 368..397
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 330
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 333
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 336
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 340
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 445 AA; 49363 MW; 928BAA0BD6767C12 CRC64;
MENNQKRQQS GMSRRSFLKV GAAATTMGVI GAIKAPAKVA NAAETLNYVP GSGKIRSKLR
PVHDFAGAKV RFVENNDQWL GTTKILTKVK MTSEADAGFM QAVRGLYGPE PQKGFFQFIA
KDPFGGSISW ARNLIAPEDV VDGAPEATKT PIPDPEQMSQ HIRDCCYFLR ADEVGIGKMP
EYGYYTHHVA DTVGLMTKPV EECVTPVTKI YPNVIVVMID QGIETMWAST GYDGISGAMS
MKSYFTSGCI AVILAKYIRT LGYNARAHHA KNYEAIMPVC IMAAGLGELS RTGDSAIHPR
LGFRHKVAAV TTDLPLAPDQ PLDFGLLDFC RVCKKCADNC PNEAISFDED PIEYNGYLRW
NSDFRKCTEF RTTNEEGSSC GTCMKVCPWN SKEDSWFHKA GVWVGSKGET ASTFLKSIDD
IFGYGTETIE KYKWWLEWPE KYVMK
